STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
EHA63004.1PFAM: Ferredoxin; KEGG: pmt:PMT1184 hypothetical protein. (101 aa)    
Predicted Functional Partners:
EHA63034.1
Sucraseferredoxin family protein; PFAM: Sucraseferredoxin-like; KEGG: pmf:P9303_08641 ferredoxin.
  
 0.990
EHA59327.1
4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; PFAM: 4Fe-4S binding domain; KEGG: pmf:P9303_23001 Fe-S-cluster-containing hydrogenase components 2.
 
 0.988
EHA59278.1
KEGG: pmt:PMT1777 ferredoxin-dependent glutamate synthase; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
     
 0.929
gcvP
Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
   
 
 0.909
EHA63429.1
4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
  
 0.902
ndhI
NAD(P)H-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family.
  
 0.902
EHA63003.1
Protein of unknown function DUF6 transmembrane; PFAM: Drug/metabolite transporter; KEGG: pmt:PMT0918 integral membrane protein, DUF6.
 
     0.799
EHA62030.1
PFAM: Molybdopterin oxidoreductase; Molybdopterin oxidoreductase, Fe4S4 domain; Molydopterin dinucleotide-binding domain; KEGG: ava:Ava_4544 assimilatory nitrate reductase (ferredoxin) precursor; SMART: Molybdopterin oxidoreductase, Fe4S4 domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
    
 0.798
ndhA
NADH dehydrogenase (quinone); NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
  
 
 0.790
ndhJ
NAD(P)H-quinone oxidoreductase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
  
 
 0.786
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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